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1.

001-es BibID:BIBFORM001204
Első szerző:Bene László (biofizikus)
Cím:Colorectal carcinoma rearranges cell surface protein topology and density in CD4+ T cells / Bene L., Kanyári Z., Bodnár A., Kappelmayer J., Waldmann T. A., Vámosi G., Damjanovich L.
Dátum:2007
Megjegyzések:Previously, we described conserved protein clusters includingMHCI and II glycoproteins, ICAM-1 adhesion molecules, and interleukin- 2 and -15 receptors in lipid rafts of several human cell types. Differential protein interactions can modulate function, thus influence cell fate. Therefore, we analyzed supramolecular clusters of CD4+ T cells from draining lymph nodes and peripheral blood of colorectal carcinoma patients, and compared these to healthy controls. Superclusters of MHC I and II with IL-2/15 receptors were identified by confocal microscopy on all cell types. Flow-cytometricFRETrevealed molecular associations of these proteins with each other and withICAM-1 as well. In draining lymph nodes expression levels of all these proteins were lower, and interactions, particularly between IL-2/15 receptors and MHC molecules weakened or disappeared as compared to the control. Stimuli/local conditions can rearrange cell surface protein patterns on the same cell type in the same patient, having important implications on further function and cell fate.
Tárgyszavak:Orvostudományok Klinikai orvostudományok Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
CD4+ T cells
colorectal carcinoma
MHC I
MHC II
IL-2R
IL-15R
ICAM-1
receptor clustering
FRET
Flow cytometry
Confocal microscopy
Membrane protein association
Draining lymph node
Megjelenés:Biochemical and Biophysical Research Communications. - 361 : 1 (2007), p. 202-207. -
További szerzők:Kanyári Zsolt (1964-) (orvos) Dóczy-Bodnár Andrea (1970-) (biofizikus) Kappelmayer János (1960-) (laboratóriumi szakorvos) Waldmann, Thomas A. Vámosi György (1967-) (biofizikus) Damjanovich László (1960-) (általános sebész)
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2.

001-es BibID:BIBFORM036993
Első szerző:Borbásné Sebestyén Veronika (biofizikus)
Cím:Membrane potential influences mobility, interactions and signaling of interleukin-2 and-15 receptors in T cells / Sebestyén Veronika, Nagy Éva, Mocsár Gábor, Papp Ferenc, Hajdú Péter, Panyi György, Tóth Katalin, Thomas A. Waldmann, Damjanovich Sándor, Bodnár Andrea, Vámosi György
Dátum:2011
Tárgyszavak:Természettudományok Biológiai tudományok idézhető absztrakt
MHC I
interleukin-2 receptor
IL-15 receptor
protein cluster
FRET
IL-2 signaling
Molekuláris Medicina
Molekuláris Medicina
Megjelenés:European Biophysics Journal with Biophysics Letters. - 40 : 1 (2011), p. 86. -
További szerzők:Nagy Éva (1980-) (molekuláris biológus) Mocsár Gábor (1981-) (biofizikus) Papp Ferenc (1979-) (biofizikus) Hajdu Péter (1975-) (biofizikus) Panyi György (1966-) (biofizikus) Tóth Katalin Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus) Dóczy-Bodnár Andrea (1970-) (biofizikus) Vámosi György (1967-) (biofizikus)
Pályázati támogatás:K77600
OTKA
TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
Receptor tirozin kinázok mint terápiás célpontok: működésük szabályozásának, és a közöttük fellépő molekuláris kölcsönhatások vizsgálata
TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
K+ csatornák élettani szerepe az immunrendszer sejtjeiben
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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3.

001-es BibID:BIBFORM005177
Első szerző:de Bakker, Bärbel I.
Cím:Nanometer-scale organization of the alpha subunits of the receptors for IL2 and IL15 in human T lymphoma cells / de Bakker, B. I., Bodnar, A., van Dijk, E. M. H. P., Vamosi, G., Damjanovich, S., Waldmann, T. A., van Hulst, N. F., Jenei, A., Garcia-Parajo, M. F.
Dátum:2008
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Cells
Human
Lymphoma
Biophysics
Hungary
egyetemen (Magyarországon) készült közlemény
Megjelenés:Journal of Cell Science. - 121 : 5 (2008), p. 627-633. -
További szerzők:Dóczy-Bodnár Andrea (1970-) (biofizikus) Dijk, Erik M. H. P., van Vámosi György (1967-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus) Waldmann, Thomas A. Hulst, Niek F., van Jenei Attila (1966-) (biofizikus) Garcia-Parajo, Maria F.
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4.

001-es BibID:BIBFORM005175
Első szerző:Dóczy-Bodnár Andrea (biofizikus)
Cím:A biophysical approach to IL-2 and IL-15 receptor function : localization, conformation and interactions / Bodnar, A., Nizsaloczki, E., Mocsar, G., Szaloki, N., Waldmann, T. A., Damjanovich, S., Vamosi, G.
Dátum:2008
Megjegyzések:Interleukin-2 and interleukin-15 (IL-2, IL-15) are key participants in T and NK cell activation and function. Sharing the beta and gamma receptor subunits results in several common functions: e.g. the promotion of T cell proliferation. On the other hand, due to their distinct alpha receptor subunits, they also play opposing roles in immune processes such as activation induced cell death and immunological memory. Divergence of signaling pathways must ensue already at the plasma membrane where the cytokines interact with their receptors. Therefore understanding molecular details of receptor organization and mapping interactions with other membrane proteins that might influence receptor conformation and function, are of key importance. Biophysical/advanced microscopic methods (fluorescence resonance energy transfer (FRET), fluorescence crosscorrelation spectroscopy (FCCS), near-field scanning optical microscopy (NSOM), X-ray crystallography, surface plasmon resonance, NMR spectroscopy) have been instrumental in clarifying the details of receptor structure and organization from the atomic level to the assembly and dynamics of supramolecular clusters. In this short review some important contributions shaping our current view of IL-2 and IL-15 receptors are presented.
Tárgyszavak:Orvostudományok Elméleti orvostudományok Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
analysis
Antibodies
Apoptosis
Biophysics
blood
Carcinoma
Cell Differentiation
Cell Fusion
Cell Line
Cell Membrane
Cell Proliferation
Cells
Complement
Confocal microscopy
Dendritic Cells
Diffusion
Energy Transfer
Epidermal Growth Factor
Fibroblasts
Fluorescence
Fluorescence correlation spectroscopy
Fluorescence Resonance Energy Transfer
FRET
Homeostasis
Human
Hungary
IL-2 and IL-15 receptors
In Vitro
Insulin
Interleukin-15
Interleukin-2
Kinetics
Lymphocytes
Lymphoma
Melanoma
Membrane Microdomains
Membrane Proteins
metabolism
methods
Mice
Microscopy
Near-field scanning optical microscopy
Phagocytosis
Phosphorylation
Photobleaching
Protein-protein interactions
Proteins
Receptor patterns
Research
Signal Transduction
Structure determination
Support
therapy
transmembrane signaling
Tyrosine
X-ray crystallography
Megjelenés:Immunology Letters. - 116 : 2 (2008), p. 117-125. -
További szerzők:Nizsalóczki Enikő Mocsár Gábor (1981-) (biofizikus) Szalóki Nikoletta (1981-) (biológus) Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus) Vámosi György (1967-) (biofizikus)
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elektronikus változat
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5.

001-es BibID:BIBFORM097487
Első szerző:Kenesei Ádám
Cím:IL-15 Trans-Presentation Is an Autonomous, Antigen-Independent Process / Kenesei Ádám, Volkó Julianna, Szalóki Nikoletta, Mocsár Gábor, Jambrovics Károly, Balajthy Zoltán, Bodnár Andrea, Tóth Katalin, Waldmann Thomas A., Vámosi György
Dátum:2021
ISSN:0022-1767 1550-6606
Megjegyzések:IL-15 plays a pivotal role in the long-term survival of T cells and immunological memory. Its receptor consists of three subunits (IL-15R?, IL-2/15R?, and ?c). IL-15 functions mainly via trans-presentation (TP), during which an APC expressing IL-15 bound to IL-15R? presents the ligand to the ??c receptor-heterodimer on a neighboring T/NK cell. To date, no direct biophysical evidence for the intercellular assembly of the IL-15R heterotrimer exists. Ag presentation (AP), the initial step of T cell activation, is also based on APC?T cell interaction. We were compelled to ask whether AP has any effect on IL-15 TP or whether they are independent processes. In our human Raji B cell?Jurkat T cell model system, we monitored inter-/intracellular protein interactions upon formation of IL-15 TP and AP receptor complexes by Förster resonance energy transfer measurements. We detected enrichment of IL-15R? and IL-2/15R? at the synapse and positive Förster resonance energy transfer efficiency if Raji cells were pretreated with IL-15, giving direct biophysical evidence for IL-15 TP. IL-15R? and MHC class II interacted and translocated jointly to the immunological synapse when either ligand was present, whereas IL-2/15R? and CD3 moved independently of each other. IL-15 TP initiated STAT5 phosphorylation in Jurkat cells, which was not further enhanced by AP. Conversely, IL-15 treatment slightly attenuated Ag-induced phosphorylation of the CD3? chain. Our studies prove that in our model system, IL-15 TP and AP can occur independently, and although AP enhances IL-15R assembly, it has no significant effect on IL-15 signaling during TP. Thus, IL-15 TP can be considered an autonomous, Ag-independent process.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
interleukin
trans-presentation
immunology
Megjelenés:Journal Of Immunology. - 207 : 10 (2021), p. 2489-2500. -
További szerzők:Volkó Julianna (1983-) (biotechnológus) Szalóki Nikoletta (1981-) (biológus) Mocsár Gábor (1981-) (biofizikus) Jambrovics Károly (1988-) (biológus, gyógyszer-biotechnológus) Balajthy Zoltán (1957-) (biokémikus, sejtbiológus) Dóczy-Bodnár Andrea (1970-) (biofizikus) Tóth Katalin Ágnes (1977-) (biokémikus, molekuláris biológus) Waldmann, Thomas A. Vámosi György (1967-) (biofizikus)
Pályázati támogatás:GINOP-2.3.2-15-2016-00026
GINOP
EFOP-3.6.3-VEKOP-16-2017-00009
EFOP
Tempus Public Foundation 273478
Egyéb
Deutscher Akademischer Austauschdienst 273478
Egyéb
HHS | NIH | National Cancer Institute intramural research program
Egyéb
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6.

001-es BibID:BIBFORM039514
Első szerző:Matkó János (biológus)
Cím:GPI-microdomains (membrane rafts) and signaling of the multi-chain interleukin-2 receptor in human lymphoma/leukemia T cell lines / Matko, J., Bodnar, A., Vereb, G., Bene, L., Vamosi, G., Szentesi, G., Szollosi, J., Gaspar, R., Horejsi, V., Waldmann, T. A., Damjanovich, S.
Dátum:2002
ISSN:0014-2956
Megjegyzések:Subunits (alpha, beta and gamma) of the interleukin-2 receptor complex (IL-2R) are involved in both proliferative and activation-induced cell death (AICD) signaling of T cells. In addition, the signaling beta and gamma chains are shared by other cytokines (e.g. IL-7, IL-9, IL-15). However, the molecular mechanisms responsible for recruiting/sorting the alpha chains to the signaling chains at the cell surface are not clear. Here we show, in four cell lines of human adult T cell lymphoma/leukemia origin, that the three IL-2R subunits are compartmented together with HLA glycoproteins and CD48 molecules in the plasma membrane, by means of fluorescence resonance energy transfer (FRET), confocal microscopy and immuno-biochemical techniques. In addition to the beta and gamma(c) chains constitutively expressed in detergent-resistant membrane fractions (DRMs) of T cells, IL-2Ralpha (CD25) was also found in DRMs, independently of its ligand-occupation. Association of CD25 with rafts was also confirmed by its colocalization with GM-1 ganglioside. Depletion of membrane cholesterol using methyl-beta-cyclodextrin substantially reduced co-clustering of CD25 with CD48 and HLA-DR, as well as the IL-2 stimulated tyrosine-phosphorylation of STATs (signal transducer and activator of transcription). These data indicate a GPI-microdomain (raft)-assisted recruitment of CD25 to the vicinity of the signaling beta and gamma(c) chains. Rafts may promote rapid formation of a high affinity IL-2R complex, even at low levels of IL-2 stimulus, and may also form a platform for the regulation of IL-2 induced signals by GPI-proteins (e.g. CD48). Based on these data, the integrity of these GPI-microdomains seems critical in signal transduction through the IL-2R complex.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:European Journal Of Biochemistry. - 269 : 4 (2002), p. 1199-1208. -
További szerzők:Dóczy-Bodnár Andrea (1970-) (biofizikus) Vereb György (1965-) (biofizikus, orvos) Bene László (1963-) (biofizikus) Vámosi György (1967-) (biofizikus) Szentesi Gergely (1976-) (kémia-fizika tanár) Szöllősi János (1953-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Horejsi, Václav Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus)
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7.

001-es BibID:BIBFORM065104
035-os BibID:(WoS)000380371400013 (Scopus)84993661764
Első szerző:Mocsár Gábor (biofizikus)
Cím:MHC I expression regulates co-clustering and mobility of interleukin-2 and -15 receptors in T cells / G. Mocsár, J. Volkó, D. Rönnlund, J. Widengren, P. Nagy, J. Szöllősi, K. Tóth, C. K. Goldman, S. Damjanovich, T. A. Waldmann, A. Bodnár, G. Vámosi
Dátum:2016
ISSN:0006-3495
Megjegyzések:MHC glycoproteins form supramolecular clusters with interleukin-2 and -15 receptors in lipid rafts of T cells.The role of highly expressed MHC I in maintaining these clusters is unknown. We knocked down MHC I inFT7.10 human T cells, and studied protein clustering at two hierarchic levels: molecular aggregations andmobility by FRET and fluorescence correlation spectroscopy, and segregation into larger domains orsuperclusters by superresolution STED microscopy. FCS based molecular brightness analysis revealed thatthe studied molecules diffused as tight aggregates of several proteins of a kind. Knockdown reduced thenumber of MHC I containing molecular aggregates and their average MHC I content, and decreased theheteroassociation of MHC I with IL-2R?/IL-15R?. The mobility of not only MHC I but also that of IL-2R?/IL-15R? increased, corroborating the general size decrease of tight aggregates. A multifaceted analysis of STEDimages revealed that the diameter of MHC I superclusters diminished from 400-600 to 200-300 nm, whereasthose of IL-2R?/IL-15R? hardly changed. MHC I and IL-2R?/IL-15R? colocalized with GM1 gangliosiderichlipid rafts, but MHC I clusters retracted to smaller subsets of GM1- and IL-2R?/IL-15R?-rich areas uponknockdown. Our results prove that changes in expression level may significantly alter the organization andmobility of interacting membrane proteins.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Biophysical Journal. - 111 : 1 (2016), p. 100-112. -
További szerzők:Volkó Julianna (1983-) (biotechnológus) Rönnlund, Daniel Widengren, Jerker Nagy Péter (1971-) (biofizikus) Szöllősi János (1953-) (biofizikus) Tóth Katalin (Heidelberg) Goldman, Caroline K. Damjanovich Sándor (1936-2017) (biofizikus) Waldmann, Thomas A. Dóczy-Bodnár Andrea (1970-) (biofizikus) Vámosi György (1967-) (biofizikus)
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8.

001-es BibID:BIBFORM075364
035-os BibID:(WoS)000432700300024 (Scopus)85046862526
Első szerző:Nagy Éva (molekuláris biológus)
Cím:Membrane Potential Distinctly Modulates Mobility and Signaling of IL-2 and IL-15 Receptors in T Cells / Éva Nagy, Gábor Mocsár, Veronika Sebestyén, Julianna Volkó, Ferenc Papp, Katalin Tóth, Sándor Damjanovich, György Panyi, Thomas A. Waldmann, Andrea Bodnár, György Vámosi
Dátum:2018
ISSN:0006-3495
Megjegyzések:The high electric ?eld across the plasma membrane might in?uence the conformation and behavior of transmembrane proteins that have uneven charge distributions in or near their transmembrane regions. Membrane depolarization of T cells occurs in the tumor microenvironment and in in?amed tissues because of K ? release from necrotic cells and hypoxia affecting the expression of K ? channels. However, little attention has been given to the effect of membrane potential (MP) changes on membrane receptor function. Therefore, we studied the in?uence of membrane de- and hyperpolarization on the biophysical properties and signaling of interleukin-2 (IL-2) and interleukin-15 (IL-15) receptors, which play important roles in T cell function. We investigated the mobility, clustering, and signaling of these receptors and major histocompatibility complex (MHC) I/II glycoproteins forming coclusters in lipid rafts of T cells. Depolarization by high K ? buffer or K channel blockers resulted in a decrease in the mobility of IL-2Ra and MHC glycoproteins, as shown by ?uorescence correlation spectroscopy, whereas hyperpolarization by the K ? ionophore valinomycin increased their mobility. Contrary to this, the mobility of IL-15Ra decreased upon both de- and hyperpolarization. These changes in protein mobility are not due to an alteration of membrane ?uidity, as evidenced by ?uorescence anisotropy measurements. Fo ? rster resonance energy transfer measurements showed that most homo- or heteroassociations of IL-2R, IL-15R, and MHC I did not change considerably, either. MP changes modulated signaling by the two cytokines in distinct ways: depolarization caused a signi?cant increase in the IL-2-induced phosphorylation of signal transducer and activator of transcription 5, whereas hyperpolarization evoked a decrease only in the IL-15-induced signal. Our data imply that the MP may be an important modulator of interleukin receptor signaling and dynamics. Enhanced IL-2 signaling in depolarized T reg ? cells highly expressing IL-2R may contribute to suppression of antitumor immune surveillance
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Biophysical Journal. - 114 : 10 (2018), p. 2473-2482. -
További szerzők:Mocsár Gábor (1981-) (biofizikus) Borbásné Sebestyén Veronika (1990-) (biofizikus) Volkó Julianna (1983-) (biotechnológus) Papp Ferenc (1979-) (biofizikus) Tóth Katalin (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus) Panyi György (1966-) (biofizikus) Waldmann, Thomas A. Dóczy-Bodnár Andrea (1970-) (biofizikus) Vámosi György (1967-) (biofizikus)
Pályázati támogatás:GINOP-2.3.2-15-2016-00026
GINOP
GINOP-2.3.3-15-2016-00003
GINOP
GINOP-2.3.3-15-2016-00030
GINOP
K103965
OTKA
EFOP-3.6.1-16-2016-00022
EFOP
K119417
OTKA
TÁMOP-4.2.4.A/2-11/1-2012-0001
TÁMOP
EFOP-3.6.3-VEKOP-16-2017-00009
EFOP
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9.

001-es BibID:BIBFORM076128
035-os BibID:(Wos)000450299400006 (Scopus)85055751019
Első szerző:Nizsalóczki Enikő
Cím:Minimum degree of overlap between IL-9R and IL-2R on human T lymphoma cells : a quantitative CLSM and FRET analysis / Nizsalóczki Enikő, Nagy Péter, Mocsár Gábor, Szabó Ágnes, Csomós István, Waldmann Thomas A., Vámosi György, Mátyus László, Bodnár Andrea
Dátum:2018
ISSN:1552-4922 1552-4930
Megjegyzések:The heterodimeric receptor complex of IL-9 consists of the cytokine-speci?c ?-subunit and the common ? -chain shared with other cytokines, including IL-2, a central regulator of T cell function. We have shown previously the bipartite spatial relationship of IL-9 and IL-2 receptors at the surface of human T lymphoma cells: in addition to common clusters, expression of the two receptor kinds could also be observed in segregated membrane areas. Here we analyzed further the mutual cell surface organization of IL-9 and IL-2 receptors. Complementing Pearson correlation data with co-occurrence analysis of confocal microscopic images revealed that a minimum degree of IL-9R/IL-2R co-localization exists at the cell surface regardless of the overall spatial correlation of the two receptor kinds. Moreover, our FRET experiments demonstrated molecular scale assemblies of the elements of the IL-9/IL-2R system. Binding of IL-9 altered the structure and/or composition of these clusters. It is hypothesized, that by sequestering receptor subunits in common membrane areas, the overlapping domains of IL-9R and IL-2R provide a platform enabling both the formation of the appropriate receptor complex as well as subunit sharing between related cytokines.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
IL-9 and -2 receptors
uorescence resonance energy transfer
Manders coef-cient
co-occurrence analysis
Pearson correlation analysis
confocal microscopy
human T lymphoma cells
co-localization of membrane proteins
Megjelenés:Cytometry Part A. - 93 : 11 (2018), p. 1106-1117. -
További szerzők:Nagy Péter (1971-) (biofizikus) Mocsár Gábor (1981-) (biofizikus) Nagyné Szabó Ágnes Timea (1982-) (vegyész) Csomós István (1983-) (molekuláris biológus) Waldmann, Thomas A. Vámosi György (1967-) (biofizikus) Mátyus László (1956-) (biofizikus) Dóczy-Bodnár Andrea (1970-) (biofizikus)
Pályázati támogatás:EFOP-3.6.3-VEKOP-16-2017-00009
EFOP
GINOP-2.3.2-15-2016-00026
GINOP
GINOP-2.3.3-15-2016-00003
GINOP
K120302
OTKA
Intramural research program of the National Cancer Institute, NIH
Egyéb
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10.

001-es BibID:BIBFORM057902
Első szerző:Nizsalóczki Enikő
Cím:Distinct spatial relationship of the interleukin-9 receptor with interleukin-2 receptor and major histocompatibility complex glycoproteins in human T lymphoma cells / Enikő Nizsalóczki, István Csomós, Péter Nagy, Zsolt Fazekas, Carolyn K. Goldman, Thomas A. Waldmann, Sándor Damjanovich, György Vámosi, László Mátyus, Andrea Bodnár
Dátum:2014
ISSN:1439-4235
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
confocal microscopy
membrane proteins
FRET
protein protein interactions
receptors
Molekuláris Medicina
Doktori iskola
Megjelenés:Chemphyschem. - 15 : 18 (2014), p. 3969-3978. -
További szerzők:Csomós István (1983-) (molekuláris biológus) Nagy Péter (1971-) (biofizikus) Fazekas Zsolt (1971-) (biofizikus) Goldman, Caroline K. Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus) Vámosi György (1967-) (biofizikus) Mátyus László (1956-) (biofizikus) Dóczy-Bodnár Andrea (1970-) (biofizikus)
Pályázati támogatás:TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
Sejtfelszíni fehérjék szerveződése: az MHC I. szerepe
TÁMOP-4.2.2/B-10/1-2010-0024
TÁMOP
Molekuláris Orvostudomány Doktori Iskola
TÁMOP-4.2.2.A-11/1/KONV-2012-0023
TÁMOP
TÁMOP-4.2.2.A-11/1/KONV-2012-0025
TÁMOP
TÁMOP-4.2.4.A/2-11/1-2012-0001
TÁMOP
CK 78179
OTKA
K 103965
OTKA
K 103906
OTKA
NK 101337
OTKA
Baross Gábor Program REG-EA-09-1-2009-0010
Egyéb
Internal Research Program of the University of Debrecen RH/885/2013
Egyéb
Intramural Research Program of the National Cancer Institute, National Institutes of Health
Egyéb
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DOI
Intézményi repozitóriumban (DEA) tárolt változat
Borító:

11.

001-es BibID:BIBFORM004736
Első szerző:Panyi György (biofizikus)
Cím:Colocalization and nonrandom distribution of Kv1.3 potassium channels and CD3 molecules in the plasma membrane of human T lymphocytes / Panyi, G., Bagdany, M., Bodnar, A., Vamosi, G., Szentesi, G., Jenei, A., Matyus, L., Varga, S., Waldmann, T. A., Gaspar, R., Damjanovich, S.
Dátum:2003
ISSN:027-8424 (Print)
Megjegyzések:Distribution and lateral organization of Kv1.3 potassium channels and CD3 molecules were studied by using electron microscopy, confocal laser scanning microscopy, and fluorescence resonance energy transfer. Immunogold labeling and electron microscopy showed that the distribution of FLAG epitope-tagged Kv1.3 channels (Kv1.3/FLAG) significantly differs from the stochastic Poisson distribution in the plasma membrane of human T lymphoma cells. Confocal laser scanning microscopy images showed that Kv1.3/FLAG channels and CD3 molecules accumulated in largely overlapping membrane areas. The numerical analysis of crosscorrelation of the spatial intensity distributions yielded a high correlation coefficient (C = 0.64). A different hierarchical level of molecular proximity between Kv1.3/FLAG and CD3 proteins was reported by a high fluorescence resonance energy transfer efficiency (E = 51%). These findings implicate that reciprocal regulation of ion-channel activity, membrane potential, and the function of receptor complexes may contribute to the proper functioning of the immunological synapse.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
analysis
Animals
Antigens, CD3
Biophysics
biosynthesis
Cell Membrane
Cells
chemistry
Electrophysiology
Energy Transfer
Epitopes
Fluorescence
Fluorescence Resonance Energy Transfer
Human
Humans
Hungary
Immunohistochemistry
immunology
Jurkat Cells
Kv1.3 Potassium Channel
Lymphocytes
Lymphoma
metabolism
Mice
Microscopy
Microscopy, Confocal
Microscopy, Electron
Models, Statistical
Potassium
Potassium Channels
Potassium Channels, Voltage-Gated
Proteins
Research
Support
T-Lymphocytes
Transfection
Megjelenés:Proceedings of the National Academy of Sciences of the United States of America. - 100 : 5 (2003), p. 2592-2597. -
További szerzők:Bagdány Miklós Dóczy-Bodnár Andrea (1970-) (biofizikus) Vámosi György (1967-) (biofizikus) Szentesi Gergely (1976-) (kémia-fizika tanár) Jenei Attila (1966-) (biofizikus) Mátyus László (1956-) (biofizikus) Varga Sándor (1943-) (biofizikus) Waldmann, Thomas A. Gáspár Rezső (1944-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:DOI
elektronikus változat
Borító:

12.

001-es BibID:BIBFORM046092
Első szerző:Vámosi György (biofizikus)
Cím:IL-2 and IL-15 receptor [alfa]-subunits are coexpressed in a supramolecular receptor cluster in lipid rafts of T cells / Vamosi G., Bodnar A., Vereb G., Jenei A., Goldman C. K., Langowski J., Toth K., Matyus L., Szollosi J., Waldmann T. A., Damjanovich S.
Dátum:2004
ISSN:0027-8424
Megjegyzések:The private alpha-chains of IL-2 and IL-15 receptors (IL-2R and IL-15R) share the signaling beta- and gamma(c)-subunits, resulting in both common and contrasting roles of IL-2 and IL-15 in T cell function. Knowledge of the cytokine-dependent subunit assembly is indispensable for understanding the paradox of distinct signaling capacities. By using fluorescence resonance energy transfer and confocal microscopy, we have shown that IL-2R alpha, IL-15R alpha, IL-2/15R beta and gamma(c)-subunits, as well as MHC class I and II glycoproteins formed supramolecular receptor clusters in lipid rafts of the T lymphoma line Kit 225 FT7.10. Fluorescence crosscorrelation microscopy demonstrated the comobility of IL-15R alpha with IL-2R alpha and MHC class I. A model was generated for subunit switching between IL-2R alpha and IL-15R alpha upon the binding of the appropriate cytokine resulting in the formation of high-affinity heterotrimeric receptors. This model suggests a direct role for the alpha-subunits, to which no definite function has been assigned so far, in tuning cellular responses to IL-2 or IL-15. In addition, both alpha-chains were at least partially homodimerized/oligomerized, which could be the basis of distinct signaling pathways by the two cytokines.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Proceedings Of The National Academy Of Sciences Of The United States Of America. - 101 : 30 (2004), p. 11082-11087. -
További szerzők:Dóczy-Bodnár Andrea (1970-) (biofizikus) Vereb György (1965-) (biofizikus, orvos) Jenei Attila (1966-) (biofizikus) Goldman, Caroline K. Langowski, Jörg Tóth Katalin (biofizikus) Mátyus László (1956-) (biofizikus) Szöllősi János (1953-) (biofizikus) Waldmann, Thomas A. Damjanovich Sándor (1936-2017) (biofizikus)
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DOI
Intézményi repozitóriumban (DEA) tárolt változat
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